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SMT3 Suppressor of Mif Two 3 Homolog 2/3 (SUMO2/3) (AA 49-81), (C-Term) antibody

Details for Product No. ABIN388034, Supplier: Log in to see
Antigen
  • SUMO2
Epitope
AA 49-81, C-Term
19
15
7
6
3
2
2
2
2
2
1
1
1
Reactivity
Human, Mouse (Murine)
120
27
24
22
2
2
1
1
Host
Rabbit
69
49
2
Clonality (Clone)
Polyclonal ()
Conjugate
Un-conjugated
5
5
4
4
4
3
3
3
3
3
3
3
3
3
3
3
3
1
1
1
1
1
1
1
1
1
1
Application
Immunohistochemistry (Paraffin-embedded Sections) (IHC (p)), Western Blotting (WB)
102
57
53
45
43
28
27
26
22
11
Supplier
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Immunogen This SUMO2/3 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 49-81 AA from the C-terminal region of human SUMO2/3.
Clone RB00635
Isotype Ig
Specificity This SUMO2/3 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 58~88 amino acids within C-terminal region of human SUMO2/3.
Predicted Reactivity Cow (Bovine),Chicken,Hamster,Pig (Porcine),Monkey,Rat (Rattus),Xenopus laevis,Zebrafish
Purification This antibody is purified through a protein A column, followed by peptide affinity purification.
Alternative Name SUMO2/3
Background SUMO2 and SUMO3 are members of the SUMO (small ubiquitin-like modifier) protein family. This protein family functions in a manner similar to ubiquitin in that it is bound to target proteins as part of a post-translational modification system. However, unlike ubiquitin which targets proteins for degradation, this protein is involved in a variety of cellular processes, such as nuclear transport, transcriptional regulation, apoptosis, and protein stability. In vertebrates, three members of the SUMO family have been described, SUMO 1 and the functionally distinct homologues SUMO 2 and SUMO 3. SUMO modification sites present in the N terminal regions of SUMO 2 and SUMO 3 are utilized by SAE1/SAE2 (SUMO E1) and Ubc9 (SUMO E2) to form polymeric chains of SUMO 2 and SUMO 3 on protein substrates, a property not shared by SUMO 1.
Synonyms: Small ubiquitin-like modifier, Ubiquitin-like protein SMT3B, Sentrin 2, HSMT3
Molecular Weight 11637 DA
Gene ID 6612
UniProt P55854
Research Area Apoptosis/Necrosis, Translation Factors, Protein Modifications, Transcription Factors, Signaling, Cell Structure
Application Notes WB = 1:1000, IHC (p) = 1:50-100
Restrictions For Research Use only
Format Liquid
Concentration 0.5 mg/mL
Buffer PBS with 0.09 % (W/V) sodium azide
Preservative Sodium azide
Precaution of Use This product contains sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Storage 4 °C/-20 °C
Storage Comment Maintain refrigerated at 2-8 °C for up to 6 months. For long term storage store at -20 °C in small aliquots to prevent freeze-thaw cycles.
Expiry Date 6 months
Supplier Images
Western Blotting (WB) image for anti-SMT3 Suppressor of Mif Two 3 Homolog 2/3 (SUMO2/3) (AA 49-81), (C-Term) antibody (ABIN388034) The anti-SUMO2/3 C-term Pab (ABIN388034) is used in Western blot to detect SUMO2/3 in...
Western Blotting (WB) image for anti-SMT3 Suppressor of Mif Two 3 Homolog 2/3 (SUMO2/3) (AA 49-81), (C-Term) antibody (ABIN388034) COS-7 cells were transfected for 24 hrs with a plasmid expressing DYKDDDDK-ERM (left ...
Immunohistochemistry (IHC) image for anti-SMT3 Suppressor of Mif Two 3 Homolog 2/3 (SUMO2/3) (AA 49-81), (C-Term) antibody (ABIN388034) Formalin-fixed and paraffin-embedded human cancer tissue reacted with the primary ant...
Product cited in: Higginbotham, OShea: "Adenovirus E4-ORF3 Targets PIAS3 and Together with E1B-55K Remodels SUMO Interactions in the Nucleus and at Virus Genome Replication Domains." in: Journal of virology, Vol. 89, Issue 20, pp. 10260-72, 2015 (PubMed).

Heo, Lee, Nigro, Thomas, Le, Chang, McClain, Reinhart-King, King, Berk, Fujiwara, Woo, Abe: "PKC? mediates disturbed flow-induced endothelial apoptosis via p53 SUMOylation." in: The Journal of cell biology, Vol. 193, Issue 5, pp. 867-84, 2011 (PubMed).

Nadtochiy, Redman, Rahman, Brookes: "Lysine deacetylation in ischaemic preconditioning: the role of SIRT1." in: Cardiovascular research, Vol. 89, Issue 3, pp. 643-9, 2011 (PubMed).

Snider, Weerasinghe, Iñiguez-Lluhí, Herrmann, Omary: "Keratin hypersumoylation alters filament dynamics and is a marker for human liver disease and keratin mutation." in: The Journal of biological chemistry, Vol. 286, Issue 3, pp. 2273-84, 2011 (PubMed).

Cho, Yi, Tserentsoodol, Searle, Ferreira: "Neuroprotection resulting from insufficiency of RANBP2 is associated with the modulation of protein and lipid homeostasis of functionally diverse but linked pathways in response to oxidative stress." in: Disease models & mechanisms, Vol. 3, Issue 9-10, pp. 595-604, 2010 (PubMed).

Martin, Schwamborn, Urlaub, Gan, Guan, Dejean: "Spatial interplay between PIASy and FIP200 in the regulation of signal transduction and transcriptional activity." in: Molecular and cellular biology, Vol. 28, Issue 8, pp. 2771-81, 2008 (PubMed).

Degerny, Monte, Beaudoin, Jaffray, Portois, Hay, de Launoit, Baert: "SUMO modification of the Ets-related transcription factor ERM inhibits its transcriptional activity." in: The Journal of biological chemistry, Vol. 280, Issue 26, pp. 24330-8, 2005 (PubMed).

Background publications Strausberg, Feingold, Grouse, Derge, Klausner, Collins, Wagner, Shenmen, Schuler, Altschul, Zeeberg, Buetow, Schaefer, Bhat, Hopkins, Jordan, Moore, Max, Wang, Hsieh, Diatchenko, Marusina, Farmer et al.: "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. ..." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 99, Issue 26, pp. 16899-903, 2002 (PubMed).

Lapenta, Chiurazzi, van der Spek, Pizzuti, Hanaoka, Brahe: "SMT3A, a human homologue of the S. cerevisiae SMT3 gene, maps to chromosome 21qter and defines a novel gene family." in: Genomics, Vol. 40, Issue 2, pp. 362-6, 1997 (PubMed).